Iron in PDB 2nuk: Soluble Domain of the Rieske Iron-Sulfur Protein From Rhodobacter Sphaeroides
Enzymatic activity of Soluble Domain of the Rieske Iron-Sulfur Protein From Rhodobacter Sphaeroides
All present enzymatic activity of Soluble Domain of the Rieske Iron-Sulfur Protein From Rhodobacter Sphaeroides:
1.10.2.2;
Protein crystallography data
The structure of Soluble Domain of the Rieske Iron-Sulfur Protein From Rhodobacter Sphaeroides, PDB code: 2nuk
was solved by
D.Kolling,
J.Brunzelle,
S.Lhee,
A.R.Crofts,
S.K.Nair,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
11.67 /
1.20
|
Space group
|
I 4
|
Cell size a, b, c (Å), α, β, γ (°)
|
70.568,
70.568,
54.769,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
11.8 /
13.6
|
Iron Binding Sites:
The binding sites of Iron atom in the Soluble Domain of the Rieske Iron-Sulfur Protein From Rhodobacter Sphaeroides
(pdb code 2nuk). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Soluble Domain of the Rieske Iron-Sulfur Protein From Rhodobacter Sphaeroides, PDB code: 2nuk:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 2nuk
Go back to
Iron Binding Sites List in 2nuk
Iron binding site 1 out
of 2 in the Soluble Domain of the Rieske Iron-Sulfur Protein From Rhodobacter Sphaeroides
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Soluble Domain of the Rieske Iron-Sulfur Protein From Rhodobacter Sphaeroides within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe200
b:8.3
occ:1.00
|
FE1
|
A:FES200
|
0.0
|
8.3
|
1.0
|
S1
|
A:FES200
|
2.2
|
9.5
|
1.0
|
S2
|
A:FES200
|
2.2
|
9.3
|
1.0
|
SG
|
A:CYS149
|
2.3
|
8.9
|
1.0
|
SG
|
A:CYS129
|
2.3
|
7.3
|
1.0
|
FE2
|
A:FES200
|
2.7
|
9.7
|
1.0
|
HB3
|
A:CYS149
|
3.0
|
8.8
|
1.0
|
HB3
|
A:CYS129
|
3.1
|
7.0
|
1.0
|
CB
|
A:CYS129
|
3.1
|
6.9
|
1.0
|
CB
|
A:CYS149
|
3.1
|
8.8
|
1.0
|
HB3
|
A:HIS131
|
3.2
|
9.2
|
1.0
|
HB2
|
A:CYS129
|
3.2
|
7.0
|
1.0
|
HB2
|
A:CYS134
|
3.4
|
9.3
|
1.0
|
HB2
|
A:CYS151
|
3.4
|
11.2
|
1.0
|
HB2
|
A:CYS149
|
3.5
|
8.8
|
1.0
|
HB2
|
A:SER154
|
3.7
|
8.7
|
1.0
|
HG
|
A:SER154
|
3.8
|
8.8
|
0.0
|
H
|
A:HIS152
|
3.8
|
11.2
|
1.0
|
H
|
A:LEU132
|
3.9
|
9.8
|
1.0
|
H
|
A:CYS134
|
4.1
|
8.8
|
1.0
|
CB
|
A:HIS131
|
4.1
|
9.2
|
1.0
|
HB2
|
A:HIS131
|
4.3
|
9.2
|
1.0
|
H
|
A:HIS131
|
4.3
|
8.2
|
1.0
|
H
|
A:CYS151
|
4.3
|
11.2
|
1.0
|
CB
|
A:CYS134
|
4.3
|
9.0
|
1.0
|
ND1
|
A:HIS131
|
4.4
|
10.0
|
1.0
|
CB
|
A:CYS151
|
4.4
|
11.1
|
1.0
|
H
|
A:SER154
|
4.4
|
9.2
|
1.0
|
OG
|
A:SER154
|
4.5
|
9.0
|
1.0
|
ND1
|
A:HIS152
|
4.5
|
11.8
|
1.0
|
CA
|
A:CYS149
|
4.5
|
8.8
|
1.0
|
HH
|
A:TYR156
|
4.5
|
6.2
|
0.0
|
CB
|
A:SER154
|
4.5
|
8.5
|
1.0
|
N
|
A:HIS152
|
4.6
|
11.2
|
1.0
|
CA
|
A:CYS129
|
4.6
|
6.8
|
1.0
|
O
|
A:CYS149
|
4.7
|
9.9
|
1.0
|
HB1
|
A:ALA167
|
4.7
|
8.6
|
1.0
|
N
|
A:LEU132
|
4.7
|
9.7
|
1.0
|
CG
|
A:HIS131
|
4.7
|
9.5
|
1.0
|
H
|
A:GLY133
|
4.7
|
9.4
|
1.0
|
C
|
A:CYS149
|
4.7
|
9.5
|
1.0
|
N
|
A:CYS134
|
4.7
|
8.8
|
1.0
|
HB2
|
A:HIS152
|
4.8
|
11.6
|
1.0
|
HB3
|
A:CYS134
|
4.8
|
9.3
|
1.0
|
HB3
|
A:CYS151
|
4.8
|
11.2
|
1.0
|
HA
|
A:CYS149
|
4.8
|
8.8
|
1.0
|
N
|
A:CYS151
|
4.9
|
11.1
|
1.0
|
HA
|
A:CYS129
|
4.9
|
6.8
|
1.0
|
HE1
|
A:TYR156
|
4.9
|
6.0
|
1.0
|
|
Iron binding site 2 out
of 2 in 2nuk
Go back to
Iron Binding Sites List in 2nuk
Iron binding site 2 out
of 2 in the Soluble Domain of the Rieske Iron-Sulfur Protein From Rhodobacter Sphaeroides
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Soluble Domain of the Rieske Iron-Sulfur Protein From Rhodobacter Sphaeroides within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe200
b:9.7
occ:1.00
|
FE2
|
A:FES200
|
0.0
|
9.7
|
1.0
|
ND1
|
A:HIS152
|
2.1
|
11.8
|
1.0
|
ND1
|
A:HIS131
|
2.1
|
10.0
|
1.0
|
S1
|
A:FES200
|
2.2
|
9.5
|
1.0
|
S2
|
A:FES200
|
2.2
|
9.3
|
1.0
|
FE1
|
A:FES200
|
2.7
|
8.3
|
1.0
|
HB3
|
A:HIS131
|
2.8
|
9.2
|
1.0
|
HB2
|
A:HIS152
|
2.9
|
11.6
|
1.0
|
CE1
|
A:HIS152
|
3.1
|
12.0
|
1.0
|
CG
|
A:HIS152
|
3.1
|
11.7
|
1.0
|
CE1
|
A:HIS131
|
3.1
|
10.3
|
1.0
|
CG
|
A:HIS131
|
3.1
|
9.5
|
1.0
|
HE1
|
A:HIS152
|
3.2
|
12.1
|
1.0
|
HE1
|
A:HIS131
|
3.3
|
10.1
|
1.0
|
H
|
A:HIS152
|
3.4
|
11.2
|
1.0
|
HB2
|
A:CYS151
|
3.4
|
11.2
|
1.0
|
CB
|
A:HIS152
|
3.4
|
11.7
|
1.0
|
CB
|
A:HIS131
|
3.4
|
9.2
|
1.0
|
H
|
A:LEU132
|
3.5
|
9.8
|
1.0
|
HB2
|
A:LEU132
|
3.7
|
11.2
|
1.0
|
N
|
A:HIS152
|
3.7
|
11.2
|
1.0
|
HG2
|
A:PRO166
|
3.8
|
11.5
|
1.0
|
HB2
|
A:HIS131
|
3.9
|
9.2
|
1.0
|
HB3
|
A:CYS151
|
4.0
|
11.2
|
1.0
|
CA
|
A:HIS152
|
4.1
|
11.3
|
1.0
|
CB
|
A:CYS151
|
4.1
|
11.1
|
1.0
|
N
|
A:LEU132
|
4.1
|
9.7
|
1.0
|
NE2
|
A:HIS152
|
4.2
|
12.9
|
1.0
|
CD2
|
A:HIS152
|
4.2
|
12.8
|
1.0
|
NE2
|
A:HIS131
|
4.2
|
11.2
|
1.0
|
HB3
|
A:HIS152
|
4.2
|
11.6
|
1.0
|
HD11
|
A:LEU132
|
4.2
|
12.8
|
1.0
|
CD2
|
A:HIS131
|
4.2
|
10.8
|
1.0
|
HG
|
A:SER154
|
4.3
|
8.8
|
0.0
|
C
|
A:CYS151
|
4.4
|
11.2
|
1.0
|
SG
|
A:CYS129
|
4.4
|
7.3
|
1.0
|
HG
|
A:LEU132
|
4.4
|
12.4
|
1.0
|
CB
|
A:LEU132
|
4.5
|
11.2
|
1.0
|
HG3
|
A:PRO166
|
4.5
|
11.5
|
1.0
|
SG
|
A:CYS149
|
4.6
|
8.9
|
1.0
|
CG
|
A:PRO166
|
4.6
|
11.6
|
1.0
|
CA
|
A:HIS131
|
4.7
|
8.8
|
1.0
|
CA
|
A:CYS151
|
4.8
|
11.0
|
1.0
|
C
|
A:HIS152
|
4.8
|
11.3
|
1.0
|
C
|
A:HIS131
|
4.8
|
9.6
|
1.0
|
HB2
|
A:CYS134
|
4.8
|
9.3
|
1.0
|
CG
|
A:LEU132
|
4.9
|
12.4
|
1.0
|
CA
|
A:LEU132
|
4.9
|
10.1
|
1.0
|
HA
|
A:HIS152
|
4.9
|
11.3
|
1.0
|
HE2
|
A:HIS152
|
5.0
|
13.4
|
0.0
|
HE2
|
A:HIS131
|
5.0
|
11.5
|
0.0
|
CD1
|
A:LEU132
|
5.0
|
12.9
|
1.0
|
OG
|
A:SER154
|
5.0
|
9.0
|
1.0
|
|
Reference:
D.J.Kolling,
J.S.Brunzelle,
S.Lhee,
A.R.Crofts,
S.K.Nair.
Atomic Resolution Structures of Rieske Iron-Sulfur Protein: Role of Hydrogen Bonds in Tuning the Redox Potential of Iron-Sulfur Clusters. Structure V. 15 29 2007.
ISSN: ISSN 0969-2126
PubMed: 17223530
DOI: 10.1016/J.STR.2006.11.012
Page generated: Sun Aug 4 00:46:03 2024
|